ID A0A1D8BZZ1_9PSEU Unreviewed; 712 AA.
AC A0A1D8BZZ1;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=BKA25_001885 {ECO:0000313|EMBL:MBB5907569.1};
OS Actinoalloteichus hymeniacidonis.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Actinoalloteichus.
OX NCBI_TaxID=340345 {ECO:0000313|EMBL:MBB5907569.1, ECO:0000313|Proteomes:UP000551592};
RN [1] {ECO:0000313|EMBL:MBB5907569.1, ECO:0000313|Proteomes:UP000551592}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45092 {ECO:0000313|EMBL:MBB5907569.1,
RC ECO:0000313|Proteomes:UP000551592};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (AUG-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-
CC Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-
CC (1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-
CC cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-
CC D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl
CC diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+);
CC Xref=Rhea:RHEA:23708, Rhea:RHEA-COMP:9602, Rhea:RHEA-COMP:9603,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58405, ChEBI:CHEBI:60033,
CC ChEBI:CHEBI:78435; EC=2.4.1.129;
CC Evidence={ECO:0000256|ARBA:ARBA00023988};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:MBB5907569.1}.
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DR EMBL; JACHIS010000001; MBB5907569.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1D8BZZ1; -.
DR STRING; 340345.TL08_17815; -.
DR Proteomes; UP000551592; Unassembled WGS sequence.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.3810.10; Biosynthetic peptidoglycan transglycosylase-like; 1.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR001264; Glyco_trans_51.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR036950; PBP_transglycosylase.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF33; PEPTIDOGLYCAN GLYCOSYLTRANSFERASE; 1.
DR Pfam; PF00912; Transgly; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
PE 4: Predicted;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645,
KW ECO:0000313|EMBL:MBB5907569.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670}.
FT DOMAIN 71..260
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 377..654
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 712 AA; 75674 MW; 6360D1DD8FAEDD47 CRC64;
MPAVFLARAK GLSKLLGLCL IAGVLVAAVL FPVAAGFGAV SNQAAETVNN TSAEVEERLP
ATNTKVTDKD GNVIAHLFHQ NRVIVGADAI SEQMKAAIVA VEDRRFEEHD GVDWQATVRV
ALQNQMSGEI EGGGSTLTQQ YVKNYLAFVV ADGDPENPEY AAATETTIAR KLREARIALD
LEKRMTKDEI LAGYLNVVPY GNEIFGVHQA AEAYFSTTPD KLTVSQSALL AAIVNAPSSL
NPIRRPEQAL ERRNVVIQLM ADQGRFSEDG PEENQRIADE IKQEGLGVGE TLNQTYNGCV
GAGTGHINGF FCSYVVNYLV EHGFDLDEIK RGGYTIQTTL DARATDAAKQ AAEHHVPKNA
DGVANVMAVV EPGTESHKVR ALVANRDYGV DPAQYQTQID LPSYVTTFGA GSIYKVFTAA
AALERGYKIG QQLDVPEVYT SNTYRGPNGP YQVRNASQNL PEQMSLTDAL AKSPNTPFIA
MQEDIGVGAV VDMASRLGLR EGMNEVNLSG TAIQPDSPDG RLNQSQGDAV TNGNQGSFTL
GAGPTGVLEL ANVSATLVSG GVWCPPTPIE EIRDRNGNVV PIDEAPCEQA VDKGLADSMV
VAMSKDTAPG GTAVNAATNA GWNRPMLGKT GTTQNYASAA FIGATPQYAG ANLIFGDTPS
PQPLCNGNPP HLCQSGNMYG GNVPARTWFD TMNVLHDGLE TAPLPAAHPR YS
//